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1B82

PRISTINE RECOMB. LIGNIN PEROXIDASE H8

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0016690molecular_functiondiarylpropane peroxidase activity
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046274biological_processlignin catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0000302biological_processresponse to reactive oxygen species
B0004601molecular_functionperoxidase activity
B0006979biological_processresponse to oxidative stress
B0016690molecular_functiondiarylpropane peroxidase activity
B0020037molecular_functionheme binding
B0034599biological_processcellular response to oxidative stress
B0042744biological_processhydrogen peroxide catabolic process
B0046274biological_processlignin catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1351
ChainResidue
AASP48
AGLY66
AASP68
ASER70
AHOH455
AHOH558

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1352
ChainResidue
AILE199
AASP201
ASER177
AASP194
ATHR196

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 2351
ChainResidue
BASP48
BGLY66
BASP68
BSER70
BHOH569
BHOH570

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 2352
ChainResidue
BSER177
BASP194
BTHR196
BILE199
BASP201

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 350
ChainResidue
AHIS39
AGLU40
AILE42
AARG43
APHE46
AILE85
AGLU146
AMET172
ALEU173
AALA175
AHIS176
AALA179
AALA180
AVAL181
AASN182
AASP183
APHE193
AILE235
ASER237
AHOH362
AHOH412
AHOH443
AHOH457
AHOH487

site_idAC6
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 350
ChainResidue
BHIS39
BGLU40
BILE42
BARG43
BPHE46
BILE85
BGLU146
BPRO147
BMET172
BLEU173
BALA175
BHIS176
BALA179
BALA180
BVAL181
BASN182
BASP183
BPHE193
BILE235
BSER237
BHOH361
BHOH416
BHOH463
BHOH521
BHOH535

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. ELVWMLSAHSV
ChainResidueDetails
AGLU168-VAL178

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. AHesIRLvFHDS
ChainResidueDetails
AALA38-SER49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS47
BHIS47

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AASP48
BASP48
BGLY66
BASP68
BSER70
BSER177
BASP194
BTHR196
BILE199
BASP201
AGLY66
AASP68
ASER70
ASER177
AASP194
ATHR196
AILE199
AASP201

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS176
BHIS176

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG43
BARG43

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN257
BASN257

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AHIS47
AASN84
AARG43

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
BHIS47
BASN84
BARG43

222036

PDB entries from 2024-07-03

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